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EGFR — PTK2

Pathways - manually collected, often from reviews:

• OpenBEL Selventa BEL large corpus: PTK2 → EGFR (increases, PTK2 Activity)
  Evidence: This is taken from supplemental table 2 from PMID 15951569 Cut-offs were 2.25 for increase and 0.5 for decrease LLID were found by converting from GI assession numbers in DAVID Spreadsheet is saved in the project folder for Cell Signaling Project # bduckworth
• KEGG Focal adhesion: EGFR/ERBB2/FLT1/FLT4/IGF1R/KDR/MET/PDGFRA/PDGFRB → PTK2 (protein-protein, activation)
• WikiPathways Focal Adhesion: BLK/EGFR/ERBB2/FGR/FLT1/HCK/IGF1R/KDR/MET/PDGFRA/PDGFRB/PTK6/SRMS/TXK/TESK2/STYK1/TNK2/TNK1 → PTK2 (activation)

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Bind_translation Interaction: EGFR — PTK2 (coimmunoprecipitation) Lu et al., Mol Cell Biol 2001*
• IRef Biogrid Interaction: EGFR — PTK2 (physical association, affinity chromatography technology) Sieg et al., Nat Cell Biol 2000*
• IRef Hprd Interaction: PTK2 — EGFR (in vitro) Sieg et al., Nat Cell Biol 2000*
• IRef Hprd Interaction: PTK2 — EGFR (in vivo) Sieg et al., Nat Cell Biol 2000*
• IRef Intact Interaction: Complex of 23 proteins (association, anti bait coimmunoprecipitation) Thelemann et al., Mol Cell Proteomics 2005
• IRef Intact Interaction: Complex of 70 proteins (association, anti bait coimmunoprecipitation) Thelemann et al., Mol Cell Proteomics 2005
• IRef Ophid Interaction: PTK2 — EGFR (aggregation, interologs mapping) Brown et al., Bioinformatics 2005
• STRING interaction: EGFR — PTK2 (interaction, mapped from kegg_pathways)
• STRING interaction: EGFR — PTK2 (interaction, mapped from kegg_pathways)
• STRING interaction: PTK2 — EGFR (interaction, mapped from kegg_pathways)
• STRING interaction: PTK2 — EGFR (interaction, mapped from kegg_pathways)

Text-mined interactions from Literome

Poppleton et al., Arch Biochem Biophys 2000 : A peptide betaIII-2 corresponding to amino acids Arg259-Lys273 in the beta2-adrenergic receptor which competes for association of Galpha ( s ) with the EGFR and increases protein tyrosine kinase activity of the EGFR could mimic the effects of EGFR-13
Kawanabe et al., Am J Physiol Heart Circ Physiol 2002 : ET-1 induced EGFR PTK transactivation was completely inhibited by AG-1478, which is a specific inhibitor of EGFR PTK ... In the absence of extracellular Ca ( 2+ ), the magnitude of EGFR PTK transactivation was near the basal level ... Based on sensitivity to nifedipine, which is a specific blocker of voltage operated Ca ( 2+ ) channels ( VOCCs ), VOCCs have minor roles in EGFR PTK transactivation ... In contrast, Ca ( 2+ ) influx through VICCs plays an important role in EGFR PTK transactivation ... In summary, Ca ( 2+ ) influx through VICCs plays an essential role in ET-1 induced EGFR PTK transactivation in rabbit internal carotid artery vascular smooth muscle cells
Sini et al., Clin Cancer Res 2005 (Neoplasms, Experimental) : Both ErbB inhibitors significantly enhanced the antitumor activity of PTK787/ZK222584
King et al., J Biol Chem 1986 : The possible role of epidermal growth factor (EGF) receptor phosphorylation at threonine 654 in modulating the protein-tyrosine kinase activity of EGF treated A431 cells has been studied
Sherrill et al., Biochemistry 1996 : The binding of epidermal growth factor (EGF) to epidermal growth factor receptor ( EGF receptor ) induces dimerization of the receptor and activation of its protein tyrosine kinase